SEPT8_HUMAN
ID SEPT8_HUMAN Reviewed; 483 AA.
AC Q92599; A6NC65; A6NKP6; F6W7K9; Q8IX36; Q8IX37; Q9BVB3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Septin-8 {ECO:0000305};
GN Name=SEPTIN8 {ECO:0000312|HGNC:HGNC:16511};
GN Synonyms=KIAA0202 {ECO:0000303|PubMed:12023038}, SEPT8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SEPTIN5, AND
RP TISSUE SPECIFICITY.
RX PubMed=12023038; DOI=10.1016/s0014-5793(02)02749-7;
RA Blaeser S., Jersch K., Hainmann I., Wunderle D., Zgaga-Griesz A., Busse A.,
RA Zieger B.;
RT "Human septin-septin interaction: CDCrel-1 partners with KIAA0202.";
RL FEBS Lett. 519:169-172(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING,
RP INTERACTION WITH SEPTIN5, AND TISSUE SPECIFICITY.
RX PubMed=12909369; DOI=10.1016/s0378-1119(03)00635-8;
RA Blaeser S., Jersch K., Hainmann I., Zieger W., Wunderle D., Busse A.,
RA Zieger B.;
RT "Isolation of new splice isoforms, characterization and expression analysis
RT of the human septin SEPT8 (KIAA0202).";
RL Gene 312:313-320(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10704283; DOI=10.1006/geno.1999.6100;
RA Wenderfer S.E., Slack J.P., McCluskey T.S., Monaco J.J.;
RT "Identification of 40 genes on a 1-Mb contig around the IL-4 cytokine
RT family gene cluster on mouse chromosome 11.";
RL Genomics 63:354-373(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 122-483 (ISOFORMS 2/3).
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP IDENTIFICATION OF INITIATOR METHIONINE.
RX PubMed=12475938; DOI=10.1091/mbc.e02-07-0438;
RA Macara I.G., Baldarelli R., Field C.M., Glotzer M., Hayashi Y., Hsu S.-C.,
RA Kennedy M.B., Kinoshita M., Longtine M., Low C., Maltais L.J., McKenzie L.,
RA Mitchison T.J., Nishikawa T., Noda M., Petty E.M., Peifer M., Pringle J.R.,
RA Robinson P.J., Roth D., Russell S.E.H., Stuhlmann H., Tanaka M., Tanaka T.,
RA Trimble W.S., Ware J., Zeleznik-Le N.J., Zieger B.;
RT "Mammalian septins nomenclature.";
RL Mol. Biol. Cell 13:4111-4113(2002).
RN [10]
RP INTERACTION WITH CDK14.
RX PubMed=12098780;
RA Yang T., Gao Y.K., Chen J.Y.;
RT "KIAA0202, a human septin family member, interacting with hPFTAIRE1.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:520-525(2002).
RN [11]
RP FUNCTION, INTERACTION WITH SEPTIN4, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15116257; DOI=10.1160/th03-09-0578;
RA Blaeser S., Horn J., Wuermell P., Bauer H., Struempell S., Nurden P.,
RA Pagenstecher A., Busse A., Wunderle D., Hainmann I., Zieger B.;
RT "The novel human platelet septin SEPT8 is an interaction partner of
RT SEPT4.";
RL Thromb. Haemost. 91:959-966(2004).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=15915442; DOI=10.1002/path.1789;
RA Hall P.A., Jung K., Hillan K.J., Russell S.E.H.;
RT "Expression profiling the human septin gene family.";
RL J. Pathol. 206:269-278(2005).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP FUNCTION (ISOFORM 4), ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=27084579; DOI=10.1242/jcs.185215;
RA Kurkinen K.M., Marttinen M., Turner L., Natunen T., Maekinen P.,
RA Haapalinna F., Sarajaervi T., Gabbouj S., Kurki M., Paananen J.,
RA Koivisto A.M., Rauramaa T., Leinonen V., Tanila H., Soininen H.,
RA Lucas F.R., Haapasalo A., Hiltunen M.;
RT "SEPT8 modulates beta-amyloidogenic processing of APP by affecting the
RT sorting and accumulation of BACE1.";
RL J. Cell Sci. 129:2224-2238(2016).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May
CC play a role in platelet secretion (PubMed:15116257). Seems to
CC participate in the process of SNARE complex formation in synaptic
CC vesicles (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:B0BNF1,
CC ECO:0000269|PubMed:15116257}.
CC -!- FUNCTION: [Isoform 4]: Stabilizes BACE1 protein levels and promotes the
CC sorting and accumulation of BACE1 to the recycling or endosomal
CC compartments, modulating the beta-amyloidogenic processing of APP.
CC {ECO:0000269|PubMed:27084579}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and can associate with cellular membranes, actin
CC filaments and microtubules. GTPase activity is required for filament
CC formation (By similarity). Interacts with CDK14 (PubMed:12098780).
CC Interacts with SEPTIN5 (PubMed:12909369). Interacts with SEPTIN7 (By
CC similarity). Interacts with SEPTIN4 (PubMed:15116257). Interacts with
CC VAMP2; the interaction inhibits interaction of VAMP2 with SYP (By
CC similarity). Interacts with STX1A (By similarity).
CC {ECO:0000250|UniProtKB:B0BNF1, ECO:0000250|UniProtKB:Q8CHH9,
CC ECO:0000269|PubMed:12098780, ECO:0000269|PubMed:12909369,
CC ECO:0000269|PubMed:15116257}.
CC -!- INTERACTION:
CC Q92599; Q99719: SEPTIN5; NbExp=6; IntAct=EBI-958021, EBI-373345;
CC Q92599-3; P05067: APP; NbExp=3; IntAct=EBI-25891137, EBI-77613;
CC Q92599-3; P04271: S100B; NbExp=3; IntAct=EBI-25891137, EBI-458391;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0BNF1}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Synapse
CC {ECO:0000250|UniProtKB:B0BNF1}. Cell projection, axon
CC {ECO:0000250|UniProtKB:B0BNF1}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000250|UniProtKB:B0BNF1}. Presynapse
CC {ECO:0000250|UniProtKB:B0BNF1}. Note=Expressed in axons of immature
CC neurons, localizes to synapses in mature neurons (By similarity). In
CC platelets, found in areas surrounding alpha-granules (PubMed:15116257).
CC {ECO:0000250|UniProtKB:B0BNF1, ECO:0000269|PubMed:15116257}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=KIAA0202b {ECO:0000303|PubMed:12023038}, SEPT8_v2
CC {ECO:0000303|PubMed:12023038}, SEPT8 TV1 {ECO:0000303|PubMed:27084579};
CC IsoId=Q92599-1; Sequence=Displayed;
CC Name=2; Synonyms=KIAA0202a {ECO:0000303|PubMed:12023038}, SEPT8_v1
CC {ECO:0000303|PubMed:12023038}, KIAA0202c {ECO:0000303|PubMed:12023038},
CC SEPT8_v1* {ECO:0000303|PubMed:12023038}, SEPT8 TV2
CC {ECO:0000303|PubMed:27084579};
CC IsoId=Q92599-2; Sequence=VSP_009644;
CC Name=3; Synonyms=KIAA0202d {ECO:0000303|PubMed:12023038}, SEPT8_v3
CC {ECO:0000303|PubMed:12023038}, SEPT8 TV4 {ECO:0000303|PubMed:27084579};
CC IsoId=Q92599-3; Sequence=VSP_009643, VSP_009644;
CC Name=4; Synonyms=SEPT8 TV3 {ECO:0000303|PubMed:27084579};
CC IsoId=Q92599-4; Sequence=VSP_054085, VSP_054086;
CC -!- TISSUE SPECIFICITY: Widely expressed, including in brain, heart and
CC platelets; most abundant in aorta. Isoform 2 is expressed at low levels
CC in specific brain areas, such as occipital pole, frontal lobe, temporal
CC lobe and putamen. Isoform 1 and 3 are highly expressed in specific
CC brain areas, such as occipital pole, frontal lobe, temporal lobe and
CC putamen. Isoform 2 is highly expressed in prostate, testis and ovary.
CC Isoform 1 and isoform 3 are expressed at low levels in prostate, testis
CC and ovary. {ECO:0000269|PubMed:12023038, ECO:0000269|PubMed:12909369,
CC ECO:0000269|PubMed:15116257, ECO:0000269|PubMed:15915442,
CC ECO:0000269|PubMed:27084579}.
CC -!- MISCELLANEOUS: [Isoform 2]: KIAA0202a differs from KIAA0202c at the
CC level of the 3'-UTR. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09407.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH01329.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO13878.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO13879.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO13880.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA13193.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D86957; BAA13193.1; ALT_INIT; mRNA.
DR EMBL; AF179995; AAG09407.1; ALT_INIT; mRNA.
DR EMBL; AF440761; AAO13878.1; ALT_INIT; mRNA.
DR EMBL; AF440762; AAO13879.1; ALT_INIT; mRNA.
DR EMBL; AF440763; AAO13880.1; ALT_INIT; mRNA.
DR EMBL; AK057797; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC004775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62315.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62317.1; -; Genomic_DNA.
DR EMBL; BC001329; AAH01329.1; ALT_INIT; mRNA.
DR CCDS; CCDS43358.1; -. [Q92599-1]
DR CCDS; CCDS43359.1; -. [Q92599-4]
DR CCDS; CCDS43360.1; -. [Q92599-2]
DR CCDS; CCDS47262.1; -. [Q92599-3]
DR RefSeq; NP_001092281.1; NM_001098811.1. [Q92599-1]
DR RefSeq; NP_001092282.1; NM_001098812.1. [Q92599-4]
DR RefSeq; NP_001092283.1; NM_001098813.1. [Q92599-3]
DR RefSeq; NP_001287727.1; NM_001300798.1.
DR RefSeq; NP_001287728.1; NM_001300799.1.
DR RefSeq; NP_055961.1; NM_015146.1. [Q92599-2]
DR PDB; 6UPR; X-ray; 2.30 A; B=36-311.
DR PDB; 6WSM; X-ray; 2.45 A; A=309-429.
DR PDBsum; 6UPR; -.
DR PDBsum; 6WSM; -.
DR AlphaFoldDB; Q92599; -.
DR SMR; Q92599; -.
DR BioGRID; 116788; 60.
DR CORUM; Q92599; -.
DR IntAct; Q92599; 26.
DR MINT; Q92599; -.
DR STRING; 9606.ENSP00000367991; -.
DR GlyGen; Q92599; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92599; -.
DR PhosphoSitePlus; Q92599; -.
DR SwissPalm; Q92599; -.
DR BioMuta; SEPT8; -.
DR DMDM; 45645200; -.
DR EPD; Q92599; -.
DR jPOST; Q92599; -.
DR MassIVE; Q92599; -.
DR MaxQB; Q92599; -.
DR PaxDb; Q92599; -.
DR PeptideAtlas; Q92599; -.
DR PRIDE; Q92599; -.
DR ProteomicsDB; 28101; -.
DR ProteomicsDB; 75347; -. [Q92599-1]
DR ProteomicsDB; 75348; -. [Q92599-2]
DR ProteomicsDB; 75349; -. [Q92599-3]
DR Antibodypedia; 26134; 244 antibodies from 30 providers.
DR DNASU; 23176; -.
DR Ensembl; ENST00000296873.11; ENSP00000296873.7; ENSG00000164402.14. [Q92599-2]
DR Ensembl; ENST00000378699.6; ENSP00000367971.2; ENSG00000164402.14. [Q92599-3]
DR Ensembl; ENST00000378719.7; ENSP00000367991.2; ENSG00000164402.14. [Q92599-1]
DR Ensembl; ENST00000448933.5; ENSP00000399840.1; ENSG00000164402.14. [Q92599-3]
DR Ensembl; ENST00000458488.2; ENSP00000394766.2; ENSG00000164402.14. [Q92599-4]
DR GeneID; 23176; -.
DR KEGG; hsa:23176; -.
DR MANE-Select; ENST00000378719.7; ENSP00000367991.2; NM_001098811.2; NP_001092281.1.
DR UCSC; uc003kxr.2; human. [Q92599-1]
DR CTD; 23176; -.
DR DisGeNET; 23176; -.
DR GeneCards; SEPTIN8; -.
DR HGNC; HGNC:16511; SEPTIN8.
DR HPA; ENSG00000164402; Tissue enhanced (brain).
DR MIM; 608418; gene.
DR neXtProt; NX_Q92599; -.
DR OpenTargets; ENSG00000164402; -.
DR PharmGKB; PA134879270; -.
DR VEuPathDB; HostDB:ENSG00000164402; -.
DR eggNOG; KOG3859; Eukaryota.
DR GeneTree; ENSGT00940000156068; -.
DR HOGENOM; CLU_017718_6_4_1; -.
DR InParanoid; Q92599; -.
DR OMA; MDLVCMK; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q92599; -.
DR TreeFam; TF101080; -.
DR PathwayCommons; Q92599; -.
DR SignaLink; Q92599; -.
DR BioGRID-ORCS; 23176; 10 hits in 1021 CRISPR screens.
DR ChiTaRS; SEPT8; human.
DR GeneWiki; SEPT8; -.
DR GenomeRNAi; 23176; -.
DR Pharos; Q92599; Tbio.
DR PRO; PR:Q92599; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q92599; protein.
DR Bgee; ENSG00000164402; Expressed in middle temporal gyrus and 194 other tissues.
DR ExpressionAtlas; Q92599; baseline and differential.
DR Genevisible; Q92599; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0033157; P:regulation of intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IDA:UniProtKB.
DR GO; GO:0035542; P:regulation of SNARE complex assembly; ISS:UniProtKB.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030646; SEPT8.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884:SF54; PTHR18884:SF54; 1.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell projection;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; GTP-binding;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..483
FT /note="Septin-8"
FT /id="PRO_0000173533"
FT DOMAIN 41..307
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..58
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 103..106
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 186..189
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 411..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 320..413
FT /evidence="ECO:0000255"
FT COMPBIAS 419..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51..58
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 187..195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12909369"
FT /id="VSP_009643"
FT VAR_SEQ 429..442
FT /note="NRSDIGAHQPGMSL -> KASGWSSIYSVTIP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054085"
FT VAR_SEQ 430..483
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10704283,
FT ECO:0000303|PubMed:12909369, ECO:0000303|PubMed:9039502"
FT /id="VSP_009644"
FT VAR_SEQ 443..483
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054086"
FT CONFLICT 116..117
FT /note="Missing (in Ref. 5; AK057797)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="E -> V (in Ref. 5; AK057797)"
FT /evidence="ECO:0000305"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:6UPR"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:6UPR"
FT STRAND 82..94
FT /evidence="ECO:0007829|PDB:6UPR"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:6UPR"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:6UPR"
FT HELIX 118..135
FT /evidence="ECO:0007829|PDB:6UPR"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:6UPR"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:6UPR"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6UPR"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:6UPR"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:6UPR"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:6UPR"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:6UPR"
FT HELIX 193..210
FT /evidence="ECO:0007829|PDB:6UPR"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6UPR"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:6UPR"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6UPR"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:6UPR"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:6UPR"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:6UPR"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:6UPR"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:6UPR"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:6UPR"
FT HELIX 282..294
FT /evidence="ECO:0007829|PDB:6UPR"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:6UPR"
FT HELIX 336..406
FT /evidence="ECO:0007829|PDB:6WSM"
SQ SEQUENCE 483 AA; 55756 MW; 35E1ACF95F5DBA6B CRC64;
MAATDLERFS NAEPEPRSLS LGGHVGFDSL PDQLVSKSVT QGFSFNILCV GETGIGKSTL
MNTLFNTTFE TEEASHHEAC VRLRPQTYDL QESNVQLKLT IVDAVGFGDQ INKDESYRPI
VDYIDAQFEN YLQEELKIRR SLFDYHDTRI HVCLYFITPT GHSLKSLDLV TMKKLDSKVN
IIPIIAKADT ISKSELHKFK IKIMGELVSN GVQIYQFPTD DEAVAEINAV MNAHLPFAVV
GSTEEVKVGN KLVRARQYPW GVVQVENENH CDFVKLREML IRVNMEDLRE QTHSRHYELY
RRCKLEEMGF QDSDGDSQPF SLQETYEAKR KEFLSELQRK EEEMRQMFVN KVKETELELK
EKERELHEKF EHLKRVHQEE KRKVEEKRRE LEEETNAFNR RKAAVEALQS QALHATSQQP
LRKDKDKKNR SDIGAHQPGM SLSSSKVMMT KASVEPLNCS SWWPAIQCCS CLVRDATWRE
GFL
